phosphorylase


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Related to phosphorylase: Glycogen phosphorylase, phosphorylase phosphatase, Purine nucleoside phosphorylase

phosphorylase

 [fos-for´ĭ-lās]
an enzyme that, in the presence of inorganic phosphate, catalyzes the conversion of glycogen into glucose-1-phosphate.

phos·phor·y·lase

(fos-fōr'i-lās),
An enzyme cleaving poly(1,4-α-d-glucosyl)n with orthophosphate to form poly(1,4-α-d-glucosyl)n-1 and α-d-glucose 1-phosphate. The active form of the enzyme is a phosphorylated protein.

phosphorylase

/phos·phor·y·lase/ (fos-for´ĭ-lās)
1. any of a group of enzymes that catalyze the phosphorolysis of glycosides, transferring the cleaved glycosyl group to inorganic phosphate. When not qualified with the substrate name, the term usually denotes glycogen phosphorylase (animals) or starch phosphorylase (plants).
2. any of a group of enzymes that catalyze the transfer of a phosphate group to an organic acceptor.

phosphorylase

(fŏs′fər-ə-lās′, -lāz′)
n.
Any of a class of enzymes that catalyze the attachment of a phosphate group to another molecule.

phosphorylase

[fosfôr′ilās]
Etymology: Gk, phosphoros, bringer of light + ase, enzyme suffix
any of a group of physiologically important enzymes that catalyze reactions between phosphates and glycogen or other starch components, yielding glucose-1-phosphate.

phos·phor·y·lase

(fos-fōr'i-lās)
A phosphorylated enzyme cleaving poly(1,4-α-d-glucosyl)n with inorganic phosphate to form poly(1,4-α- d-glucosyl)n-1 and α-d-glucose 1-phosphate.

muscle enzymes

the table lists some of the most often-mentioned enzymes present in skeletal muscle, with their locations and functions. Apart from actomyosin and myosin ATPases which are associated with the contractile mechanism, they are by no means specific to muscle, being present and highly active also in other tissues. See also Krebs cycle, muscle fibre types.
Table 1: Muscle enzymes
Name SiteCatalyses…
Actomyosin ATPase (amATPase) myosin head groups hydrolysis (Mg-dependent and triggered by rise in [Ca2+]) of terminal phosphate group of ATP when head-group is in interaction with actin, releasing energy that powers force- generation. (Compare myosin ATPase)
Creatine kinase (CK) cytoplasm transfer of phosphate group from creatine phosphate to ADP, producing ATP and creatine. Isoenzymes can be distinguished in blood when either skeletal or cardiac muscle has been damaged.
Hexokinase (HK) cytoplasm 'capture' of glucose after uptake from the blood, by conversion to the impermeant glucose 6-phosphate, in type 1 muscle fibres, which utilize glucose directly.
Lactate dehydrogenase (LDH) cytoplasm reduction of pyruvate to lactate when oxygen tension is low, and the converse when it is high. Isoenzymes can be distinguished in blood when either skeletal or cardiac muscle has been damaged.
Myosin ATPase (mATPase) myosin head groups hydrolysis (Ca2+ dependent, Mg2+ independent) of terminal phosphate group of ATP by head group alone, not interacting with actin (so not contraction-producing: cf actomyosin ATPase). Basic histochemical marker for fast vs. slow fibres.
Phosphofructokinase (PFK) cytoplasm conversion of fructose 6-phosphate to fructose 1,6-diphosphate; rate-limiting for glycolysis, and sensitive to very many stimulatory and inhibitory influences.
Phosphorylase (PPL) cytoplasmremoval of hexose units, one at a time, from glycogen, to form glucose 1-phosphate: rate-limiting enzyme of, and histochemical marker for, glycogenolysis.
Pyruvate dehydrogenase (PDH) mitochondrial envelope oxidative decarboxylation of pyruvate (from cytoplasm) to form acetyl CoA, which thence feeds into tricarboxylic acid (Krebs) cycle
Sarcoplasmic reticulum ATPase (srATPase) SR membrane pumping of [Ca2+] back into SR after its electrically stimulated release
Succinate dehydrogenase (SDH) mitochondrial inner membrane oxidation of succinate to fumarate, in tricarboxylic acid (Krebs) cycle. Histochemical marker for aerobic capacity.

glycogenolysis

removal of a glucose molecule from glycogen, by the action of the enzyme glycogen phosphorylase, present in liver, kidneys, muscle and brain. The products are a glycogen molecule that is one glucose residue shorter than before and glucose-1-phosphate. This in turn is converted to glucose-6-phosphate, from which free glucose can be released from the liver and kidneys (but not from skeletal muscle or brain) by the action of glucose-6-phosphatase. See also glucose, glycolysis.

phosphorylase

a key regulatory enzyme that, in the presence of inorganic phosphate, catalyzes the removal of one glucose unit from glycogen to glucose-1-phosphate.

citrulline phosphorylase
see ornithine carbamoyl transferase.
phosphorylase kinase
an enzyme that activates phosphorylase by catalyzing the phosphorylation of serine. See also kinase.
References in periodicals archive ?
A significant decline in the glycogen level as well as in the glycogen synthase activity anda concomitant increase in the activity of glycogen phosphorylase were noted in the liver of diabetic rats.
Colorectal tumors responding to 5-fluorouracil have low gene expression levels of dihydropyrimidine dehydrogenase, thymidylate synthase, and thymidine phosphorylase.
From the data presented in the table 1, it was noticed that there is significant elevation in the glycogen phosphorylase level in the gill, muscle and liver of fish exposed to lethal and sublethal concentration of deltamethrin.
Staining with phosphorylase stain showed no activity, establishing the diagnosis of McArdle disease, as seen in Figure 3 and Figure 4.
BioCryst's lead product candidate, Fodosine(TM), is a transition-state analog inhibitor of the target enzyme purine nucleoside phosphorylase (PNP).
As the rate of glycogenolysis is regulated by glycogen phosphorylase (GP), inhibition of this key enzyme may constitute a therapeutic option for the treatment of type 2 diabetes.
In muscle cells, for example, an enzyme called phosphorylase releases stored energy.
BioCryst currently has two late-stage development programs: peramivir, a viral neuraminidase inhibitor for the treatment of influenza, and ulodesine, a purine nucleoside phosphorylase (PNP) inhibitor for the treatment of gout.
The activities of hexokinase, glucose-6-phosphatase, fructose-1,6- bisphosphatase, glucose-6-phosphate dehydrogenase, glycogen synthase and glycogen phosphorylase were measured.
About TAS-102 TAS-102 combines: FTD (alpha, alpha, alpha-trifluorothymidine), a nucleoside analog which disrupts a variety of DNA functions necessary for the proliferation of cancer cells by being efficiently incorporated into DNA, and 5-chloro-6-(2-iminopyrrolidin-1-yl)-methyl-2, 4(1H, 3H)-pyrimidinedione hydrochloride (TPI), which maintains an effective blood concentration of FTD by inhibiting thymidine phosphorylase which is the primary enzyme involved in the degradation of FTD.
Gene Gene name US patent symbol MGST3 Microsomal glutathione S-transferase 3 5,919,627 GBP1 Guanylate binding protein 1, interferon- 6,894,157 inducible, 67kDa GGH Gamma-glutamyl hydrolase (conjugase, 5,801,031 folylpolygammaglutamyl hydrolase) MTAP Methylthioadenosine phosphorylase 5,942,393; 6,870,037 MADCAM1 Mucosal vascular addressin cell adhesion 7,750,137 molecule 1 POSTN Periostin, osteoblast specific factor 6,518,063 PMS1 PMS1 postmeiotic segregation increased 1 5,922,855; (S.
Washington, June 18 (ANI): An enzyme, called human polynucleotide phosphorylase or hPNPaseold-35, discovered in 2003, could play a major role in preventing melanoma-the most serious type of skin cancer.